P39929 (SNF7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar-sorting protein SNF7

Alternative name(s):
DOA4-independent degradation protein 1
Vacuolar protein-sorting-associated protein 32

Gene names

Name:	SNF7
Synonyms:	DID1, VPS32
Ordered Locus Names:	YLR025W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Appears to sequester MVB cargo. Recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles. Ref.5 Ref.6
Subunit structure	Self-associates. Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with VTA1; the interaction requires DID2. Interacts with BRO1. Ref.6 Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Endosome membrane; Peripheral membrane protein Ref.6.
Miscellaneous	Present with 3270 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SNF7 family.
Caution	Was originally (Ref.1) thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to anoxia Inferred from mutant phenotype PubMed 20402793. Source: SGD intralumenal vesicle formation Inferred from mutant phenotype PubMed 19234443. Source: SGD late endosome to vacuole transport Inferred from mutant phenotype PubMed 9606181. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred by curator Ref.8. Source: SGD
Cellular_component	ESCRT III complex Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-17554,EBI-17554
VPS4	P52917	4	EBI-17554,EBI-20475

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 240	240	Vacuolar-sorting protein SNF7		PRO_0000211446
Regions
	Compositional bias	68 – 71	4	Poly-Lys
	Compositional bias	216 – 228	13	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	72	1	Phosphothreonine Ref.11 Ref.12 Ref.15
	Modified residue	116	1	Phosphothreonine Ref.15
	Modified residue	119	1	Phosphoserine Ref.12 Ref.15
	Modified residue	193	1	Phosphoserine Ref.15
	Modified residue	204	1	Phosphoserine Ref.15
	Modified residue	213	1	Phosphoserine Ref.13
Experimental info
	Sequence conflict	173	1	E → G in AAS56528. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P39929 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 5241A18BB181F0C1	FASTA	240	26,987
	10 20 30 40 50 60 MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE ARIFLTKGNK 70 80 90 100 110 120 VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN LETMRAMQEG AKAMKTIHSG 130 140 150 160 170 180 LDIDKVDETM DEIREQVELG DEISDAISRP LITGANEVDE DELDEELDML AQENANQETS 190 200 210 220 230 240 KIVNNNVNAA PISENKVSLP SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae." Tu J., Vallier L.G., Carlson M. Genetics 135:17-23(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins." Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M. J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting." Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D. Dev. Cell 3:271-282(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS20, SUBCELLULAR LOCATION.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae." Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H. Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRO1.
[9]	"Structural basis for endosomal targeting by the Bro1 domain." Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H. Dev. Cell 8:937-947(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRO1.
[10]	"Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body." Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H. Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VTA1.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-119, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, MASS SPECTROMETRY.
[14]	"Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation." Teis D., Saksena S., Emr S.D. Dev. Cell 15:578-589(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ASSEMBLY OF THE ESCRT-III COMPLEX.
[15]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; THR-116; SER-119; SER-193 AND SER-204, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L09751 Genomic DNA. No translation available. Z73197 Genomic DNA. Translation: CAA97548.1. AY558202 Genomic DNA. Translation: AAS56528.1. BK006945 Genomic DNA. Translation: DAA09343.1.
PIR	S52590.
RefSeq	NP_013125.1. NM_001181912.1.
3D structure databases
ProteinModelPortal	P39929.
SMR	P39929. Positions 121-175.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1747N.
IntAct	P39929. 21 interactions.
MINT	MINT-389266.
STRING	4932.YLR025W.
Proteomic databases
PaxDb	P39929.
PeptideAtlas	P39929.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR025W; YLR025W; YLR025W.
GeneID	850712.
KEGG	sce:YLR025W.
Organism-specific databases
CYGD	YLR025w.
SGD	S000004015. SNF7.
Phylogenomic databases
eggNOG	NOG291419.
GeneTree	ENSGT00390000005006.
HOGENOM	HOG000209960.
KO	K12194.
OMA	DSLMQDI.
OrthoDB	EOG4TMVBN.
Gene expression databases
Genevestigator	P39929.
GermOnline	YLR025W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005024. Snf7. [Graphical view]
Pfam	PF03357. Snf7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966772.

Entry information

Entry name

SNF7_YEAST

Accession

Primary (citable) accession number: P39929
Secondary accession number(s): D6VY27, E9P8V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program